NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|802188285|ref|WP_046051814|]
View 

methionyl-tRNA formyltransferase [Yersinia enterocolitica]

Protein Classification

methionyl-tRNA formyltransferase( domain architecture ID 11415469)

methionyl-tRNA formyltransferase catalyzes formylation of the initiator methionyl-tRNA

CATH:  3.40.50.170|3.10.25.10
EC:  2.1.2.9
Gene Ontology:  GO:0004479|GO:0071951
PubMed:  8199241

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
5-314 0e+00

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 510.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNAD 84
Cdd:COG0223    1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDPEFLEELRALNPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:COG0223   81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 165 SATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAFNPWPVSYFVVDEQ 244
Cdd:COG0223  161 AGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAFTTLDGK 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 245 PIKVWQAQVLATVDNAAPGTIIHADKHGIQVATADGVLNITQLQPAGKKAMSAADLLNSRRewFIPGNQL 314
Cdd:COG0223  241 RLKIWKARVLEEAGGGAPGTILAVDKDGLLVACGDGALRLLELQPAGKKRMSAADFLRGYR--LKPGERL 308
 
Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
5-314 0e+00

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 510.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNAD 84
Cdd:COG0223    1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDPEFLEELRALNPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:COG0223   81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 165 SATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAFNPWPVSYFVVDEQ 244
Cdd:COG0223  161 AGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAFTTLDGK 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 245 PIKVWQAQVLATVDNAAPGTIIHADKHGIQVATADGVLNITQLQPAGKKAMSAADLLNSRRewFIPGNQL 314
Cdd:COG0223  241 RLKIWKARVLEEAGGGAPGTILAVDKDGLLVACGDGALRLLELQPAGKKRMSAADFLRGYR--LKPGERL 308
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 5-314 2.05e-147

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 416.80  E-value: 2.05e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285    5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNAD 84
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAGRGKKLTPPPVKVLAEEKGIPVFQPEKQRQLEELPLVRELKPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:TIGR00460  81 VIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  165 SATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAFNPWPVSYFVVDEQ 244
Cdd:TIGR00460 161 SGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAWLTFEGK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802188285  245 PIKVWQAQVLATVDNAA-PGTIIHADKHGIQVAT-ADGVLNITQLQPAGKKAMSAADLLN-SRREWFIPGNQL 314
Cdd:TIGR00460 241 NIKIHKAKVIDLSTYKAkPGEIVYHNKKGILVACgKDGILLLLSLQPPGKKVMRAEDFYNgSRHPWYVPGSSA 313
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 5-208 9.91e-116

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187715 [Multi-domain]  Cd Length: 204  Bit Score: 332.10  E-value: 9.91e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNAD 84
Cdd:cd08646    1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPRGRGKKLTPSPVKELALELGLPVLQPEKLKDEEFLEELKALKPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:cd08646   81 LIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDT 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 802188285 165 SATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKL 208
Cdd:cd08646  161 AGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI 204
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 6-305 3.31e-69

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 218.41  E-value: 3.31e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   6 RIIFAGTPDFAARHLGALL------SSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIP---IFQPKSLRPEENQH 76
Cdd:PLN02285   8 RLVFLGTPEVAATVLDALLdasqapDSAFEVAAVVTQPPARRGRGRKLMPSPVAQLALDRGFPpdlIFTPEKAGEEDFLS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  77 LVADLNADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIE 156
Cdd:PLN02285  88 ALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQER 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 157 CDIQPEDTSATLYDKLAQLGPQGLLVTLQQLAEGSAQPE--VQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAFNPW 234
Cdd:PLN02285 168 VEVDEDIKAPELLPLLFELGTKLLLRELPSVLDGSAKDKatPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGW 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 235 P--VSYFVV----DEQP----IKVWQAQVLATV-DNAAPGTIIHADKHGIQVATADG-VLNITQLQPAGKKAMSAADLLN 302
Cdd:PLN02285 248 PgtRAKFQLvddgDGERevleLKIITTRVCEAGgEQTGSADAVTFKKDSLLVPCGGGtWLEVLEVQPPGKKVMKAKDFWN 327


                 ...
gi 802188285 303 SRR 305
Cdd:PLN02285 328 GLR 330
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 5-184 2.58e-64

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 200.60  E-value: 2.58e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285    5 LRIIFA--GTPDFAARHLGALLSSQH--QIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDipiFQPKSLRPEENQHLVAD 80
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQdaDVVLVISNKDKAAGLGRAEQAGIPTFVFEHKG---LTPRSLFDQELADALRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   81 LNADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQ 160
Cdd:pfam00551  78 LAADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPIL 157

                         170       180
                  ....*....|....*....|....
gi 802188285  161 PEDTSATLYDKLAQLGPQGLLVTL 184
Cdd:pfam00551 158 PDDTAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
5-314 0e+00

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 510.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNAD 84
Cdd:COG0223    1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDPEFLEELRALNPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:COG0223   81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 165 SATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAFNPWPVSYFVVDEQ 244
Cdd:COG0223  161 AGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAFTTLDGK 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 245 PIKVWQAQVLATVDNAAPGTIIHADKHGIQVATADGVLNITQLQPAGKKAMSAADLLNSRRewFIPGNQL 314
Cdd:COG0223  241 RLKIWKARVLEEAGGGAPGTILAVDKDGLLVACGDGALRLLELQPAGKKRMSAADFLRGYR--LKPGERL 308
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 5-314 2.05e-147

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 416.80  E-value: 2.05e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285    5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNAD 84
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAGRGKKLTPPPVKVLAEEKGIPVFQPEKQRQLEELPLVRELKPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:TIGR00460  81 VIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  165 SATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAFNPWPVSYFVVDEQ 244
Cdd:TIGR00460 161 SGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAWLTFEGK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802188285  245 PIKVWQAQVLATVDNAA-PGTIIHADKHGIQVAT-ADGVLNITQLQPAGKKAMSAADLLN-SRREWFIPGNQL 314
Cdd:TIGR00460 241 NIKIHKAKVIDLSTYKAkPGEIVYHNKKGILVACgKDGILLLLSLQPPGKKVMRAEDFYNgSRHPWYVPGSSA 313
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 5-208 9.91e-116

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187715 [Multi-domain]  Cd Length: 204  Bit Score: 332.10  E-value: 9.91e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNAD 84
Cdd:cd08646    1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPRGRGKKLTPSPVKELALELGLPVLQPEKLKDEEFLEELKALKPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:cd08646   81 LIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDT 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 802188285 165 SATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKL 208
Cdd:cd08646  161 AGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI 204
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 6-305 3.31e-69

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 218.41  E-value: 3.31e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   6 RIIFAGTPDFAARHLGALL------SSQHQIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDIP---IFQPKSLRPEENQH 76
Cdd:PLN02285   8 RLVFLGTPEVAATVLDALLdasqapDSAFEVAAVVTQPPARRGRGRKLMPSPVAQLALDRGFPpdlIFTPEKAGEEDFLS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  77 LVADLNADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIE 156
Cdd:PLN02285  88 ALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQER 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 157 CDIQPEDTSATLYDKLAQLGPQGLLVTLQQLAEGSAQPE--VQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAFNPW 234
Cdd:PLN02285 168 VEVDEDIKAPELLPLLFELGTKLLLRELPSVLDGSAKDKatPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGW 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 235 P--VSYFVV----DEQP----IKVWQAQVLATV-DNAAPGTIIHADKHGIQVATADG-VLNITQLQPAGKKAMSAADLLN 302
Cdd:PLN02285 248 PgtRAKFQLvddgDGERevleLKIITTRVCEAGgEQTGSADAVTFKKDSLLVPCGGGtWLEVLEVQPPGKKVMKAKDFWN 327


                 ...
gi 802188285 303 SRR 305
Cdd:PLN02285 328 GLR 330
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 5-184 2.58e-64

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 200.60  E-value: 2.58e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285    5 LRIIFA--GTPDFAARHLGALLSSQH--QIVGVFTQPDRPAGRGNKLTPSPVKVLAEQHDipiFQPKSLRPEENQHLVAD 80
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQdaDVVLVISNKDKAAGLGRAEQAGIPTFVFEHKG---LTPRSLFDQELADALRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   81 LNADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQ 160
Cdd:pfam00551  78 LAADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPIL 157

                         170       180
                  ....*....|....*....|....
gi 802188285  161 PEDTSATLYDKLAQLGPQGLLVTL 184
Cdd:pfam00551 158 PDDTAETLYNRVADLEHKALPRVL 181
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 7-186 1.61e-52

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.


Pssm-ID: 187712 [Multi-domain]  Cd Length: 173  Bit Score: 170.16  E-value: 1.61e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   7 IIFAGTPDFAARHLGALLSS-QHQIVGVFTQPDRPAGRGnkltpspvKVLAEQHDIPIFQPKSLRPEENQHLVADLNADI 85
Cdd:cd08369    1 IVILGSGNIGQRVLKALLSKeGHEIVGVVTHPDSPRGTA--------QLSLELVGGKVYLDSNINTPELLELLKEFAPDL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  86 MVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDTS 165
Cdd:cd08369   73 IVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTA 152

                        170       180
                 ....*....|....*....|.
gi 802188285 166 ATLYDKLAQLGPQGLLVTLQQ 186
Cdd:cd08369  153 GTLYQRLIELGPKLLKEALQK 173
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 7-288 6.87e-47

bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 167.08  E-value: 6.87e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   7 IIFAgTPDFAARHLGALLSSQHQIVGVFTQPDRPagrGNKLTPSPVKVLAEQHDIPIFQPkslrpEENQHL-----VADL 81
Cdd:PRK08125   4 VVFA-YHDIGCVGIEALLAAGYEIAAVFTHTDNP---GENHFFGSVARLAAELGIPVYAP-----EDVNHPlwverIREL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  82 NADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQP 161
Cdd:PRK08125  75 APDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 162 EDTSATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAF-NPWPVSYFV 240
Cdd:PRK08125 155 DDTALTLHHKLCHAARQLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAVtDPWPGAFSY 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 802188285 241 VDEQPIKVWQAQVLATVDNAAPGTIIHADKhgIQVATADGVLNITQLQ 288
Cdd:PRK08125 235 VGEQKFTVWSSRVLPDASGAQPGTVLSVAP--LRIACGEGALEIVTGQ 280
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
207-305 1.14e-40

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 137.41  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  207 KLSKEEAKLDWSLPAVQLERCIRAFNPWPVSYFVVDEQPIKVWQAQVLATVDNAAPGTIIHADKHGIQVATADGVLNITQ 286
Cdd:pfam02911   1 KIKKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKASVLDQESGAAPGTIVTVDKGGLLVACGDGALLILE 80

                          90
                  ....*....|....*....
gi 802188285  287 LQPAGKKAMSAADLLNSRR 305
Cdd:pfam02911  81 LQLEGKKPMSAEDFLNGFR 99
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 6-204 1.26e-40

ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.


Pssm-ID: 187713 [Multi-domain]  Cd Length: 203  Bit Score: 140.56  E-value: 1.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   6 RIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPagrGNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNADI 85
Cdd:cd08644    2 KAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNP---GENIWFGSVAQLAREHGIPVFTPDDINHPEWVERLRALKPDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  86 MVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDTS 165
Cdd:cd08644   79 IFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTA 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 802188285 166 ATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTY 204
Cdd:cd08644  159 KSLFHKLCVAARRLLARTLPALKAGKARERPQDETQASY 197
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 211-297 4.98e-39

C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.


Pssm-ID: 187732 [Multi-domain]  Cd Length: 87  Bit Score: 132.65  E-value: 4.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 211 EEAKLDWSLPAVQLERCIRAFNPWPVSYFVVDEQPIKVWQAQVLATVDNAAPGTIIHADKHGIQVATADGVLNITQLQPA 290
Cdd:cd08704    1 EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGKRLKILKAEVLEESGEAAPGTILAVDKKGLLVACGDGALEILELQPE 80


                 ....*..
gi 802188285 291 GKKAMSA 297
Cdd:cd08704   81 GKKRMSA 87
PRK06988 PRK06988
formyltransferase;
6-300 9.04e-38

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 136.36  E-value: 9.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   6 RIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAgrgNKLTPSPVKVLAEQHDIPIFQPKSLRPEENQHLVADLNADI 85
Cdd:PRK06988   4 RAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDNPT---ENIWFGSVAAVAAEHGIPVITPADPNDPELRAAVAAAAPDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  86 MVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQrslWA---GDAKTGVTIMQMDVGLDTGDMLHKIECDIQPE 162
Cdd:PRK06988  81 IFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVN---WAvlnGETETGATLHEMVAKPDAGAIVDQTAVPILPD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 163 DTSATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTYAEKLSKEEAKLDWSLPAVQLERCIRAF-NPWPVSYFVV 241
Cdd:PRK06988 158 DTAAQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLAQGSYFGGRKPEDGRIDWSKPAAQVYNLIRAVaPPYPGAFTDL 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802188285 242 DEQPIKVWQA----QVLATVDNAAPGtiIHADKHGIQVATADG----VLNITQLQPAGKKAMSAADL 300
Cdd:PRK06988 238 GGTRFVVARArlaaPGAAAARDLPPG--LHVSDNALFGVCGDGravsILELRRQQDGGETVVTPAQF 302
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 6-180 2.50e-32

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 118.14  E-value: 2.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   6 RIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNK-LTPSPvkvLAEQHDIPIFQPKSLRPEENQHLVADLNAD 84
Cdd:cd08651    1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSDyLDLDS---FARKNGIPYYKFTDINDEEIIEWIKEANPD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:cd08651   78 IIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDT 157

                        170
                 ....*....|....*.
gi 802188285 165 SATLYDKLAQLGPQGL 180
Cdd:cd08651  158 ANSLYDKIMEAAKQQI 173
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 5-204 1.62e-29

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 111.77  E-value: 1.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRpAGRgnkltPSPVKVLAEQHDIPIFQPKSLR------PE---ENQ 75
Cdd:cd08647    1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDK-DGK-----ADPLALEAEKDGVPVFKFPRWRakgqaiPEvvaKYK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  76 HLVADLNadimVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKI 155
Cdd:cd08647   75 ALGAELN----VLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQK 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 802188285 156 ECDIQPEDTSATLYDK-LAQLGPQGLLVTLQQLAEGSAQPEVQDEAQVTY 204
Cdd:cd08647  151 ECDVLPNDTVDTLYNRfLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATY 200
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 63-176 1.43e-19

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 83.42  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  63 IFQPKSLRPEENQHLVADLNADImVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDA-KTGVTIMQ 141
Cdd:cd08653   28 VIVVNSINGPEVVAALRALAPDV-VSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPdNVGVTVHL 106

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 802188285 142 MDVGLDTGDMLHKIECDIQPEDTSATLYDKLAQLG 176
Cdd:cd08653  107 VDAGIDTGDVLAQARPPLAAGDTLLSLYLRLYRAG 141
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 72-188 5.34e-18

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 79.80  E-value: 5.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  72 EENQHLVADLNADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDM 151
Cdd:cd08823   61 EQLAEWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPI 140

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 802188285 152 LHKIECDIQPEDTSATLYDKLAQLGPQGLLVTLQQLA 188
Cdd:cd08823  141 VLEQFTPIHPDDTYGLLCSRLAMLAVGLLEELYQNLA 177
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 5-205 3.82e-17

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 77.89  E-value: 3.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   5 LRIIFAGTPDFAARHLGALLSSQHQIVGVFTQPDRPAGRGNKLTpspvkvlAEQHDIPIFQPKSLRPEEnqhlVADlNAD 84
Cdd:cd08822    1 MKIAIAGQKWFGTAVLEALRARGIALLGVAAPEEGDRLAAAART-------AGSRGLPRAGVAVLPADA----IPP-GTD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  85 IMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDT 164
Cdd:cd08822   69 LIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDT 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 802188285 165 SATLYDK-LAQLGPQGLLVTLQQLAEGSAQPEV-QDEAQVTYA 205
Cdd:cd08822  149 AAELWRRaLAPMGVKLLTQVIDALLRGGNLPAQpQDERLATWE 191
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 22-179 1.06e-15

N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.


Pssm-ID: 187718 [Multi-domain]  Cd Length: 166  Bit Score: 73.45  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  22 ALLSSQHQIVGVFTqpdrpagrgnklTPSPVKVLAEQHDIPIFQPkslrPEENQHLVADLNADIMVVVAYGLILPASVLA 101
Cdd:cd08649   17 QLLAAGHRIAAVVS------------TDPAIRAWAAAEGIAVLEP----GEALEELLSDEPFDWLFSIVNLRILPSEVLA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802188285 102 MPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDTSATLYDKLAQLGPQG 179
Cdd:cd08649   81 LPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSLNLKCYEAGIEG 158
FMT_C_like cd08370
Carboxy-terminal domain of Formyltransferase and similar domains; This family represents the ...
 219-290 2.17e-13

Carboxy-terminal domain of Formyltransferase and similar domains; This family represents the C-terminal domain of formyltransferase and similar proteins. This domain is found in a variety of enzymes with formyl transferase and alkyladenine DNA glycosylase activities. The proteins with formyltransferase function include methionyl-tRNA formyltransferase, ArnA, 10-formyltetrahydrofolate dehydrogenase and HypX proteins. Although most proteins with formyl transferase activity contain this C-terminal domain, prokaryotic glycinamide ribonucleotide transformylase (GART), a single domain protein, only contains the core catalytic domain. Thus, the C-terminal domain is not required for formyl transferase catalytic activity and may be involved in substrate binding. Some members of this family have shown nucleic acid binding capacity. The C-terminal domain of methionyl-tRNA formyltransferase is involved in tRNA binding. Alkyladenine DNA glycosylase is a distant member of this family with very low sequence similarity to other members. It catalyzes the first step in base excision repair (BER) by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site and shows ability to bind to DNA.


Pssm-ID: 187727  Cd Length: 73  Bit Score: 64.36  E-value: 2.17e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802188285 219 LPAVQLERCIRAFnPWPVSYFVVDEQPIKVWQAQVLATVDNAA--PGTIIHADKHGIQVATADGVLNITQLQPA 290
Cdd:cd08370    1 LDAESLERTIRAL-PYQGARLEIDGERVRLLEAEVVDDVTNEArhSGKILFVDYQCITVATGDGALLITALQGL 73
Arna_FMT_C cd08702
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ...
 211-300 5.96e-12

C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.


Pssm-ID: 187730  Cd Length: 92  Bit Score: 60.72  E-value: 5.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 211 EEAKLDWSLPAVQLERCIRAFN-PWPVSYFVVDEQPIKVWQAQVLA-TVDNAAPGTIIHADKHGIQVATADGVLNITQLQ 288
Cdd:cd08702    1 EDGLIDWRMSAREIYNLVRAVTkPYPGAFTFVGGQKIKIWKARPVDdAFYNGEPGKVLSVDGDPLIVACGDGALEILEAE 80

                         90
                 ....*....|..
gi 802188285 289 PAGKKAMSAADL 300
Cdd:cd08702   81 LDGGLPLAGEQL 92
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 6-171 9.27e-12

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 62.46  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   6 RIIFAGTPDFAARHLGALLSSQH----QIVGVFTqpdrpagrgnkltpSPVKVLAEQHDIPIFQPKSLRPEENQ--HLVA 79
Cdd:cd08820    1 RIVFLGQKPIGEECLRTLLRLQDrgsfEIIAVLT--------------NTSPADVWEGSEPLYDIGSTERNLHKllEILE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  80 DLNADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDI 159
Cdd:cd08820   67 NKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPI 146

                        170
                 ....*....|..
gi 802188285 160 QPEDTSATLYDK 171
Cdd:cd08820  147 PSDCTVISLYIL 158
FMT_C_OzmH_like cd08700
C-terminal subdomain of the Formyltransferase-like domain found in OzmH-like proteins; Domain ...
 215-302 1.85e-11

C-terminal subdomain of the Formyltransferase-like domain found in OzmH-like proteins; Domain found in OzmH-like proteins with similarity to the C-terminal domain of Formyltransferase. OzmH is one of the proteins involved in the synthesis of Oxazolomycin (OZM), which is a hybrid peptide-polyketide antibiotic that exhibits potent antitumor and antiviral activities. OzmH is a multi-domain protein consisting of a formyl transferase domain, a flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a phosphopantetheine (PP)-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.


Pssm-ID: 187728  Cd Length: 100  Bit Score: 59.55  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 215 LDWSLPAVQLERCIRA------FNPWPVSYFVVDEQPIKVWQAQVLATVDNAAPGTIIHADKHGIQVATADGVLNITQLQ 288
Cdd:cd08700    5 LDFTRPAAELSALVRAldfggyWNPLCVAKILLADRVLLVGKAEVLAVSSGGAPGTVLAVDADGWTVATGDGAVRLSGLT 84

                         90
                 ....*....|....
gi 802188285 289 PAGKKAMSAADLLN 302
Cdd:cd08700   85 DLDGAAVDLAALAQ 98
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 29-190 2.63e-11

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 61.97  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  29 QIVGVFTqpDRPAGRGNKLtpspvkvlAEQHDIP--IFQPKSL--RPEENQHLVADL---NADImVVVA-YGLILPASVL 100
Cdd:COG0299   30 EIVLVIS--NRPDAYGLER--------ARAAGIPtfVLDHKDFpsREAFDAALLEALdayGPDL-VVLAgFMRILTPEFV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 101 A--MPRLgcINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDTSATLYDKLAQLGPQ 178
Cdd:COG0299   99 RafPGRI--INIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARILEQEHR 176

                        170
                 ....*....|...
gi 802188285 179 gLLV-TLQQLAEG 190
Cdd:COG0299  177 -LYPeAIRLLAEG 188
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 56-168 9.56e-11

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 59.71  E-value: 9.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  56 AEQHDIP--IFQPKS--LRPEENQHLVADLNA---DIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSL 128
Cdd:cd08645   45 AKKAGIPtfVINRKDfpSREEFDEALLELLKEykvDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAAL 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 802188285 129 WAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDTSATL 168
Cdd:cd08645  125 EAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETL 164
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 56-192 3.14e-09

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 55.84  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285   56 AEQHDIP--IFQPKSL--RPEENQHLVADLNA---DIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSL 128
Cdd:TIGR00639  46 AAQAGIPtfVLSLKDFpsREAFDQAIIEELRAhevDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQAL 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802188285  129 WAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDTSATLYDKLAQLGPQGLLVTLQQLAEGSA 192
Cdd:TIGR00639 126 EAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGRL 189
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
107-172 6.66e-07

dTDP-4-amino-4,6-dideoxyglucose formyltransferase;


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 49.52  E-value: 6.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802188285 107 CINVHGSLLPRWRGAAPIQRSLwAGDAKTGVTIMQMDVGLDTGDMLHKIECDIQPEDTSATLYDKL 172
Cdd:PRK07579  88 CINIHPGFNPYNRGWFPQVFSI-INGLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARV 152
FMT_core_like_1 cd08821
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 94-154 1.90e-04

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187723 [Multi-domain]  Cd Length: 211  Bit Score: 41.92  E-value: 1.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802188285  94 ILPASVLAmpRLGCINVHGSLLPRWRGAAPIQRSLWAGDAKTGVTIMQMDVGLDTGDMLHK 154
Cdd:cd08821   56 IIPKEIFE--NFECVVFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYLK 114
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 55-173 7.05e-04

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 40.55  E-value: 7.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  55 LAEQHDIPIFQ----PKSLRPEENQ--HLVADLNADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSL 128
Cdd:PRK13010 136 LAVQHDIPFHHlpvtPDTKAQQEAQilDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAH 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 802188285 129 WAGDAKTGVTIMQMDVGLDTGDMlhkIECDIQPEDTSATLYDKLA 173
Cdd:PRK13010 216 ARGVKLIGATAHFVTDDLDEGPI---IEQDVERVDHSYSPEDLVA 257
FDH_Hydrolase_C cd08703
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...
 210-298 1.49e-03

The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.


Pssm-ID: 187731 [Multi-domain]  Cd Length: 100  Bit Score: 37.33  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 210 KEEAKLDWSLPAVQLERCIRAFNPWPVSYFVVDEQPI-----KVWQAQVLA----TVDNAAPGTIIHADkhGIQVATADG 280
Cdd:cd08703    1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVtlfgsSLWKGGKPPggevEVEGLERPGIVHKN--GLLITGSDG 78

                         90
                 ....*....|....*....
gi 802188285 281 V-LNITQLQPAGKKAMSAA 298
Cdd:cd08703   79 KmVNVKRLQFEDGKMIPAS 97
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 57-202 1.65e-03

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 39.34  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  57 EQHDIPIF----QPKSLRPEENQHLVADlnADIMVVVAYGLILPASVLAMPRLGCINVHGSLLPRWRGAAPIQRSLWAGD 132
Cdd:PLN02828 120 ERHGIPYHylptTKENKREDEILELVKG--TDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGV 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285 133 AKTGVTIMQMDVGLDTGDMLHKIECDIQPEDTSATLYDKLAQLGPQGLLVTLQQLAEGSAQPEVQDEAQV 202
Cdd:PLN02828 198 KLIGATSHFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAIKSYCELRVLPYGTNKTVV 267
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 55-126 3.28e-03

Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine.


Pssm-ID: 187717 [Multi-domain]  Cd Length: 196  Bit Score: 37.93  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802188285  55 LAEQHDIPIF------QPKSLRPEENQHLVADLNADIMVVVAYGLILPASVLAmpRLG--CINVHGSLLPRWRGAAPIQR 126
Cdd:cd08648   43 LAERFGIPFHhipvtkDTKAEAEAEQLELLEEYGVDLVVLARYMQILSPDFVE--RYPnrIINIHHSFLPAFKGAKPYHQ 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH